Elastin is a major component of connective tissue and is primarily responsible for elasticity inherent in aorta, large arteries and lung. An obstacle to the understanding of the pathology of elastic tissue has been a lack of understanding of the structure, development and function of a normal elastic tissue, especially the protein elastin. The aim of this proposal is directed toward eludicating the primary structure of elastin and process of elastic fibrogenesis through investigation of mature elastin peptide and peptides derived from a soluble form of elastin. Specifically we hope to 1) Establish a "normal" elastin structure from a functioning elastin tissue, 2) Characterize the crosslinked areas of insoluble elastin in order to gain insight into the particular sites of tropoelastin destined for crosslink information, 3) Examine elastin from both diseased and aged tissue for such parameters as quantity and location of crosslinks, and omissions or substitutions of primary sequences and 4) investigate and locate and binding sites of lipids, lipoproteins and glycoproteins, and Ca ion in elastin preparations from both normal and aged and/or disease specimens. Ultimately, my goal is to examine the role of elastin in arteriosclerosis by defining a normal elastin structure, comparing this to the structure of both aged and diseased elastin with a positive contribution to understanding and prevention of the above transition.